The importance of the last strand at the C-terminus in βB2-crystallin stability and assembly
Cataract-linked mutation R188H promotes βB2-crystallin aggregation and fibrillization during acid denaturation
Cataract-causing mutation R233H affects the stabilities of βB1- and βA3/βB1-crystallins with different pH-dependence
The Benefits of Being β-Crystallin Heteromers: βB1-Crystallin Protects βA3-Crystallin against Aggregation during Co-refolding
The N-Terminal Extension of βB1-Crystallin Chaperones β-Crystallin Folding and Cooperates with αA-Crystallin
